Počet záznamů: 1
Excited-state properties of the 16 kDa red carotenoid protein from Arthrospira maxima
- 1. 0352596 - BC-A 2012 RIV NL eng J - Článek v odborném periodiku
Chábera, P. - Durchan, Milan - Shih, P.M. - Kerfeld, C.A. - Polívka, Tomáš
Excited-state properties of the 16 kDa red carotenoid protein from Arthrospira maxima.
Biochimica Et Biophysica Acta-Bioenergetics. Roč. 1807, č. 1 (2011), s. 30-35 ISSN 0005-2728
Výzkumný záměr: CEZ:AV0Z50510513
Klíčová slova: cyanobacteria * carotenoid * excited-state
Kód oboru RIV: BO - Biofyzika
Impakt faktor: 4.843, rok: 2011
We have studied spectroscopic properties of the 16 kDa red carotenoid protein (RCP), which is closely related to the orange carotenoid protein (OCP) from cyanobacteria. Both proteins bind the same chromophore, the carotenoid 3′-hydroxyechinenone (hECN), and the major difference between the two proteins is lack of the C-terminal domain in the RCP; this results in exposure of part of the carotenoid. The excited-state lifetime of hECN in the RCP is 5.5 ps, which is markedly longer than in OCP (3.3 ps) but close to 6 ps obtained for hECN in organic solvent. This confirms that the binding of hECN to the C-terminal domain in the OCP changes conformation of hECN, thereby altering its excited-state properties. Hydrogen bonds between the C-terminal domain and the carotenoid are also absent in the RCP. This allows the conformation of hECN in the RCP to be similar to that in solution, which results in comparable excited-state properties of hECN in solution.
Trvalý link: http://hdl.handle.net/11104/0192071